BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15845

Title: Mouse Prion Protein (121-231) with Mutation S170N   PubMed: 18773909

Authors: Perez, Daniel; Wuthrich, Kurt

Citation: Christen, Barbara; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "NMR Structure of the Bank Vole Prion Protein at 20 degrees C Contains a Structured Loop of Residues 165-171"  J. Mol. Biol. 383, 306-312 (2008).

Assembly members:
Prion_Protein, polymer, 114 residues, Formula weight is not available

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Prion_Protein: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYNNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts135
1H chemical shifts396

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prion Protein1

Entities:

Entity 1, Prion Protein 114 residues - Formula weight is not available

1   GLYSERVALVALGLYGLYLEUGLYGLYTYR
2   METLEUGLYSERALAMETSERARGPROMET
3   ILEHISPHEGLYASNASPTRPGLUASPARG
4   TYRTYRARGGLUASNMETTYRARGTYRPRO
5   ASNGLNVALTYRTYRARGPROVALASPGLN
6   TYRASNASNGLNASNASNPHEVALHISASP
7   CYSVALASNILETHRILELYSGLNHISTHR
8   VALTHRTHRTHRTHRLYSGLYGLUASNPHE
9   THRGLUTHRASPVALLYSMETMETGLUARG
10   VALVALGLUGLNMETCYSVALTHRGLNTYR
11   GLNLYSGLUSERGLNALATYRTYRASPGLY
12   ARGARGSERSER

Samples:

13C_15N: Prion Protein, [U-99% 13C; U-99% 15N], 0.4 mM; D2O 10%; H2O 90%; sodium acetate, [U-2H], 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY13C_15Nisotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

CARA, Keller, Rochus - data analysis

ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking

DYANA v1.0.3, Guntert, Braun and Wuthrich - structure solution

OPAL v1.2, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker DRX 750 MHz

Related Database Links:

BMRB 15824 16071 16075 16076 16077 16078 16079 16080 16184 16185 16722 16723 17081 17082 17084 17174 17213 17758 17759
PDB
DBJ BAA08790 BAE28320 BAE28693 BAE29994 BAE34221
EMBL CAJ18553
GB AAA37013 AAA37014 AAA39996 AAA39997 AAA39998
PIR B34759
REF NP_001265185 NP_035300 NP_036763 XP_003499061 XP_006235124
SP P04925 P13852 Q60468 Q60506 Q9Z0T3